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20241105232507.0 |
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240902s2024 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2024.112241
|2 doi
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|a pubmed24n1591.xml
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|a (DE-627)NLM377038180
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|a (NLM)39216697
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|a (PII)S0168-9452(24)00268-1
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Kim, Jae Ho
|e verfasserin
|4 aut
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| 245 |
1 |
4 |
|a The RING-type E3 ligase, TaFRFP, regulates flowering by controlling a salicylic acid-mediated floral promotion
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|c 2024
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 26.10.2024
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|a Date Revised 04.11.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2024 Elsevier B.V. All rights reserved.
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|a The initiation of transition to flowering is carefully managed by endogenous and environmental cues, which is critical for flowering plant reproductive success. Here, we found that wheat RING-type E3 ligase TaFRFP was highly expressed from the double ridge to degeneration stage (WS2.5-WS9). TaFRFP is localized in the nucleus and has E3 ligase activity in vitro. TaFRFP overexpression in Arabidopsis resulted in an early flowering phenotype, but to a lesser extent, under short-day conditions. Under the SA-treated condition, overexpression of TaFRFP shows higher root growth and has more accumulation of SA contents. A proteomic comparison revealed that the amount of FRL4A protein, a FRIGIDA LIKE 4 A, was considerably lower in SA-treated TaFRFP seedlings compared to normal condition. We further found that TaFRFP directly interacts with FRL4A in the nucleus and recruits it to the FLC locus in Arabidopsis. Moreover, an ubiquitination assay showed that TaFRPF physically interact and ubiquitinates TaFRL as a substrate. Our findings support the concept that the TaFRFP E3 ligase works as a positive regulator, and that the ubiquitination of its substrate proteins plays a significant role in controlling flowering time via an SA-dependent pathway
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|a Journal Article
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|a E3 ligase
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|a Ubiquitination
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|a Wheat
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|a flowering time
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|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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|a EC 2.3.2.27
|2 NLM
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| 650 |
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|a Salicylic Acid
|2 NLM
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| 650 |
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7 |
|a O414PZ4LPZ
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Arabidopsis Proteins
|2 NLM
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| 700 |
1 |
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|a Kim, Moon Seok
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Seo, Yong Weon
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 349(2024) vom: 15. Nov., Seite 112241
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
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| 773 |
1 |
8 |
|g volume:349
|g year:2024
|g day:15
|g month:11
|g pages:112241
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| 856 |
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|u http://dx.doi.org/10.1016/j.plantsci.2024.112241
|3 Volltext
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|d 349
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|h 112241
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